Rice stripe virus utilizes a <i>Laodelphax striatellus</i> salivary carbonic anhydrase to facilitate plant infection by direct molecular interaction.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 41492962.
- Also identified by DOI 10.7554/eLife.88132 and PMC identifier 12774414.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Plant viruses typically rely on insect vectors for transmission between plants, with insect salivary proteins playing critical roles in this process. In this study, we demonstrate how <i>Laodelphax striatellus</i> salivary carbonic anhydrase (LssaCA) promotes rice stripe virus (RSV) infection in plants. We discovered that LssaCA directly binds to RSV nucleocapsid protein (NP) in insect salivary glands. This LssaCA-NP complex interacts with a rice thaumatin-like protein (OsTLP) that possesses endo-β-1,3-glucanase activity potentially degrading callose. Upon binding, the LssaCA-NP complex significantly enhances OsTLP enzymatic activity. We further clarify that both <i>L. striatellus</i> feeding and RSV infection induce callose deposition. The tripartite LssaCA-NP-OsTLP interaction enhances callose degradation, thereby facilitating RSV infection via its insect vector. This study provides new insights into complex virus-insect-plant tripartite interactions mediated by insect salivary proteins, with broad implications for numerous plant viruses transmitted by insect vectors.
Medical subject headings
- Tenuivirus
- Plant Diseases
- Hemiptera
- Carbonic Anhydrases
- Insect Proteins
- Oryza